文献详情
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
文献类型期刊论文
通讯作者Wang, CG (reprint author), Tongji Univ, Sch Life Sci & Technol, Shanghai Peoples Hosp 10, Dept Cent Lab, Shanghai 200092, Peoples R China.; Gigant, B (reprint author), Univ Paris Saclay, Univ Paris Sud, CNRS, CEA,I2BC, F-91198 Gif Sur Yvette, France.
2017
期刊名称NATURE COMMUNICATIONS影响因子和分区
8
增刊正刊
收录情况SCI(E)(WOS:000405112600001)  
所属部门医院
语言外文
ISSN2041-1723
DOI10.1038/s41467-017-00091-9
人气指数192
浏览次数192
基金Fondation ARC pour la recherche sur le cancer postdoctoral fellowship [PDF 20130606987]; National Natural Science Foundation of China [31370771]; Agence Nationale de la Recherche [ANR-12-BSV8-0002-01]; CNRS; French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
摘要Kinesin-13s are critical microtubule regulators which induce microtubule disassembly in an ATP dependent manner. To clarify their mechanism, we report here the crystal structure of a functional construct of the kinesin-13 Kif2C/MCAK in an ATP-like state and bound to the alpha beta-tubulin heterodimer, a complex mimicking the species that dissociates from microtubule ends during catalytic disassembly. Our results picture how Kif2C stabilizes a curved tubulin conformation. The Kif2C alpha 4-L12-alpha 5 region undergoes a remarkable 25 degrees rotation upon tubulin binding to target the alpha beta-tubulin hinge. This movement leads the beta 5a-beta 5b motif to interact with the distal end of beta-tubulin, whereas the neck and the KVD motif, two specific elements of kinesin-13s, target the alpha-tubulin distal end. Taken together with the study of Kif2C mutants, our data suggest that stabilization of a curved tubulin is an important contribution to the Kif2C mechanism.
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